Title page for ETD etd-050406-111437

Document Type thesis

Author Name Sands, Eric R

URN etd-050406-111437

Title Cloning and Expression of Thermophilic, Mesophilic, and Psychrophilic Zn2+ Transporting ATPases

Degree MS

Department Chemistry & Biochemistry

Advisors
José Argüello, Advisor
James Pavlik, Department Head

Keywords
Heavy metals
ATPase
Membranes
Lipids
Zn-transporter

Date of Presentation/Defense 2006-05-03

Availability unrestricted

Abstract
Protein folding and stability are essential for protein function. Changes in these characteristics can lead to altered physiological states and to the development of certain pathologies. While extensive research has focused on the stability of soluble proteins, membrane protein stability has received much less attention. Understanding the stability of membrane proteins can provide insight into folding mechanisms and the etiology of various pathologies. The purpose of this project is to prepare molecular tools to perform comparative studies of homologous membrane proteins that are found in various environments. To this end, thermophilic (Pyrococcus abyssi), mesophilic (Escherichia coli), and psychrophilic (Exiguobacterium 255-15) transmembrane Zn2+ transporting ATPases were cloned, expressed, and functionally characterized to correlate thermostability with optimal functional temperatures. In addition, the lipid environments and composition (rigid or fluid lipids) may also be involved in determining the stability of membrane proteins. Toward exploring the role of extremophilic lipids, Archaeoglobus fulgidus and Thermotoga maritima were grown and lipids were extracted. Availability of these molecular tools will enable physical-chemical studies toward understanding the structural factors that determine functional stability.

Files
EricSandsMSThesis.pdf

Browse by Author | Browse by Department | Search all available ETDs

Questions? Email etd-questions@wpi.edu
Maintained by webmaster@wpi.edu

Document Type	thesis
Author Name	Sands, Eric R
URN	etd-050406-111437
Title	Cloning and Expression of Thermophilic, Mesophilic, and Psychrophilic Zn2+ Transporting ATPases
Degree	MS
Department	Chemistry & Biochemistry
Advisors	José Argüello, Advisor James Pavlik, Department Head
Keywords	Heavy metals ATPase Membranes Lipids Zn-transporter
Date of Presentation/Defense	2006-05-03
Availability	unrestricted
Abstract Protein folding and stability are essential for protein function. Changes in these characteristics can lead to altered physiological states and to the development of certain pathologies. While extensive research has focused on the stability of soluble proteins, membrane protein stability has received much less attention. Understanding the stability of membrane proteins can provide insight into folding mechanisms and the etiology of various pathologies. The purpose of this project is to prepare molecular tools to perform comparative studies of homologous membrane proteins that are found in various environments. To this end, thermophilic (Pyrococcus abyssi), mesophilic (Escherichia coli), and psychrophilic (Exiguobacterium 255-15) transmembrane Zn2+ transporting ATPases were cloned, expressed, and functionally characterized to correlate thermostability with optimal functional temperatures. In addition, the lipid environments and composition (rigid or fluid lipids) may also be involved in determining the stability of membrane proteins. Toward exploring the role of extremophilic lipids, Archaeoglobus fulgidus and Thermotoga maritima were grown and lipids were extracted. Availability of these molecular tools will enable physical-chemical studies toward understanding the structural factors that determine functional stability.
Files	EricSandsMSThesis.pdf